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Goat polyclonal to PDE5A
This antibody is expected to recognise all 4 reported isoforms (as represented by NP_001074; NP_236914; NP_246273). [NP_237223 has been retracted].
HumanPredicted to work with:
Rat, Cow, Dog
, corresponding to C terminal amino acids 864-875 of Human PDE5A.
- Human lung lysate. Lysate prepared from transfected HEK293 cells transiently expressing PDE5A.
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Preservative: 0.02% Sodium Azide.
Constituents: 0.5% BSA, Tris saline. pH 7.3.
Concentration information loading...
Immunogen affinity purified
This antibody was purified from goat serum by ammonium sulphate precipitation, followed by antigen affinity chromatography using the immunizing peptide.
Immunizing Peptide (Blocking)
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
||Use a concentration of 0.3 - 1 µg/ml. Detects a band of approximately 100 kDa (predicted molecular weight: 100 kDa).Can be blocked with PDE5A peptide (864-875) (ab45684).
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP.
Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung.
Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
Belongs to the cyclic nucleotide phosphodiesterase family.
Contains 2 GAF domains.
Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.
Phosphorylation is regulated by binding of cGMP to the two allosteric sites.
Information by UniProt
- 5''-cyclic phosphodiesterase antibody
- CGB PDE antibody
- CGB-PDE antibody
has not yet been referenced specifically in any publications.
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